Genet. Res., Camb. (1979), 33, pp. 129-136 With 5 text-figures
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Variation among inbred strains of mice in adenosine 3': 5' cyclic monophosphate levels of spermatozoa BY ROBERT P. ERICKSON*t, MARTIN S. BUTLEY*$, SUSAN R. MARTINf§ AND CHARLES J. BETLACHfH * Department of Human Genetics, University of Michigan, Ann Arbor, Michigan 48109 and | Department of Pediatrics, University of San Francisco, California 94143 {Received 18 August 1978) SUMMARY
Spermatozoa from inbred strains of mice were found to vary significantly for levels of cyclic AMP when extractions were performed in a reproducible manner. The F x hybrid between high and low spermatozoal cAMP strains showed spermatozoal cAMP levels typical of the low strain. An analysis of spermatozoal cAMP in individual mice from the backcross of the F x to the high strain suggested that alleles at more than one locus determine strain differences in spermatozoal cAMP. The major histocompatibility locus of mice, H-2, which had been found to have an effect on liver cAMP levels did not seem to affect spermatozoal cAMP levels. ^-Alleles, which appear to alter fertilization rates by effects on motility, had no apparent affects on spermatozoal cAMP. 1. INTRODUCTION Adenosine 3': 5' cyclic monophosphate (cAMP) is believed to play a role in the induction or maintenance of sperm motility since there is a high correlation between the measured levels of cAMP and sperm motility under a variety of conditions (Hoskins & Casillas, 1975). These cAMP augmenting conditions include the addition of cyclic nucleotide phosphodiesterase inhibitors (Garbers, First & Lardy, 1973), dilution (Cascieri, Amann & Hammerstedt, 1976), and sea-urchinegg factors (Garbers & Hardman, 1976). Furthermore, most of the components of cAMP-modulated regulatory systems are found in spermatozoa (Gray et al. 1976): adenyl cyclase (Casillas & Hoskins, 1970), cyclic nucleotide phosphodiesterase (Christiansen & Desautel, 1973), cAMP-dependent protein kinase (Hoskins, Casillas & Stephens, 1972), and a phosphoprotein phosphatase which dephosphorylates proteins phosphorylated by this protein kinase (Tang & Hoskins, 1975). However, the natural stimulus for mammalian sperm adenyl cyclase (Garbers & Hardman, 1975) and the motility-coupled intermediate phosphorylated by the cAMP-dependent protein kinase (Tamblyn & First, 1977) have not been identified. As part of our studies on the genetic control of sperm function, we have studied % Current address: School of Pharmacy, University of Colorado, Boulder, Colorado. § Current address: Department of Ophthalmology, University of California, San Francisco, California. \\ Current address: College of Pharmacy, University of South Carolina, Columbia, South Carolina. 0016-6723/79/2828-7340 $0,100 ©1979 Cambridge University Press
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variations in endogenous cAMP levels among inbred strains of mice. These strains include both standard laboratory stocks and lines carrying